PDBsum entry 2vqp

Viral protein

PDB id: 2vqp

Contents

Protein chain

255 a.a. *

Ligands

GOL ×2

FMT ×7

ACT ×3

Waters ×186

* Residue conservation analysis

PDB id:

2vqp

Name:

Viral protein

Title:

Structure of the matrix protein from human respiratory syncytial virus

Structure:

Matrix protein. Chain: a. Engineered: yes. Mutation: yes

Source:

Human respiratory syncytial virus. Organism_taxid: 11259. Strain: a2. Expressed in: escherichia coli. Expression_system_taxid: 511693.

Resolution:

1.60Å R-factor: 0.182 R-free: 0.217

Authors:

V.A.Money,H.K.Mcphee,J.M.Sanderson,R.P.Yeo

Key ref:

V.A.Money et al. (2009). Surface features of a Mononegavirales matrix protein indicate sites of membrane interaction. Proc Natl Acad Sci U S A, 106, 4441-4446. PubMed id: 19251668 DOI: 10.1073/pnas.0805740106

Date:

18-Mar-08 Release date: 17-Feb-09

Protein chain

P0DOE7  (MATRX_HRSVA) -  Matrix protein from Human respiratory syncytial virus A (strain A2)

Seq: 256 a.a.

Struc: 255 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1073/pnas.0805740106

Proc Natl Acad Sci U S A 106:4441-4446 (2009)

PubMed id: 19251668

Surface features of a Mononegavirales matrix protein indicate sites of membrane interaction.

V.A.Money, H.K.McPhee, J.A.Mosely, J.M.Sanderson, R.P.Yeo.

ABSTRACT

The matrix protein (M) of respiratory syncytial virus (RSV), the prototype viral member of the Pneumovirinae (family Paramyxoviridae, order Mononegavirales), has been crystallized and the structure determined to a resolution of 1.6 A. The structure comprises 2 compact beta-rich domains connected by a relatively unstructured linker region. Due to the high degree of side-chain order in the structure, an extensive contiguous area of positive surface charge covering approximately 600 A(2) can be resolved. This unusually large patch of positive surface potential spans both domains and the linker, and provides a mechanism for driving the interaction of the protein with a negatively-charged membrane surface or other virion components such as the nucleocapsid. This patch is complemented by regions of high hydrophobicity and a striking planar arrangement of tyrosine residues encircling the C-terminal domain. Comparison of the RSV M sequence with other members of the Pneumovirinae shows that regions of divergence correspond to surface exposed loops in the M structure, with the majority of viral species-specific differences occurring in the N-terminal domain.

Selected figure(s)

Figure 2.
Comparison of the RSV M protein topology with that of EBOV VP40. The diagrams show an overlay of the β-sheet arrangements of M^254R with EBOV VP40 (PDB code 1ES6). (A) RSV M protein N-terminal domain in blue and VP40 in yellow; and (B) M^254R protein C-terminal domain in red and VP40 in cyan. The same images are presented in Fig. S2, in stereoscopic views.

Figure 5.
Distribution of tyrosine residues in the C-terminal domain of the RSV M. The N-terminal domain of M^254R has been omitted for clarity. The planar distribution of the residues (shown as ball-and-stick representations) on the surface of the M protein is readily apparent. The C-terminal residue is indicated by C; A and B show orthogonal views of this domain.

Figures were selected by an automated process.